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Dietary fibres (DF) have been isolated from rapeseed and peas, separated into different fractions and investigated for their content of associated non-carbohydrate compounds, especially proteins by UV-spectroscopy, nitrogen determination, isoelectric focusing, and rocket Immunoelectrophoresis. The level of protein varied according to the plant origin of DF and among the different DF fractions (pectins, hemicelluloses, cellulose, lignins). In general, rapeseed DF contained more protein than pea DF, with the hemicellulose fraction from rapeseed hulls having the highest level. Rocket immunoelectrophoresis proved the presence of myrosinase as part of the DF associated proteins in rapeseed. This may be of importance for the degradation of glucosinolates in the digestive tract of humans and animals, and thereby the effects from these compounds are changed.
The results of previous research on antigenic (allotypic) specificities of immunoglobulins, alpha-globulins, beta-globulins and lipoproteins in cattle are reviewed. The suitability of heteroantibodies and alloantibodies for identification of this type of markers was analysed. New names/symbols of antigenic markers of proteins in cattle, identified at the Department of Immuno- and Cytogenetics of the National Research Institute of Animal Production (Balice/Kraków, Poland), were introduced.
α-Amylase isozymes from rye endosperm were analysed by means of isoelectric focusing, polyacrylamide gel electrophoresis, immunoelectrophoresis and colorimetric assay. Α-AMY 1 (high pI) group was separated into 13 IEF bands, whereas in group α-AMY2 (low pI) 2 intensive and 6-8 faint bands were found. Two linked (2±1 cM) polymorphic loci and a single locus with two alleles encoding for α-AMY 1 and α-AMY 2 groups, respectively, were identified after genetic analysis of the IEF patterns. All α-amylase isozymes developed on PAGE, were shown to belong to α-AMY 1 group. It was demonstrated that a single PAGE isozyme corresponds to 2-4 separate IEF bands and that most of the IEF bands can be attributed to more than one PAGE isozyme. The activity of α-amylases from PAGE zone I was 2.3 times higher than the activity of zone II isozymes. A strong correlation between the activity and protein amount of particular α-AMY 1 isozymes (r=0.94) was found.
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